A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins

Yi Quan Tang, Jun Yuan, George Ösapay, Klara Ösapay, Dat Tran, Chris J Miller, Andre J. Ouellette, Michael E. Selsted

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565 Scopus citations

Abstract

Analysis of rhesus macaque leukocytes disclosed the presence of an 18- residue macrocyclic, tridisulfide antibiotic peptide in granules of neutrophils and monocytes. The peptide, termed rhesus theta defensin-1 (RTD- 1), is microbicidal for bacteria and fungi at low micromolar concentrations. Antibacterial activity of the cyclic peptide was threefold greater than that of an open-chain analog, and the cyclic conformation was required for antimicrobial activity in the presence of 150 millimolar sodium chloride. Biosynthesis of RTD-1 involves the head-to-tail ligation of two α-defensin- related nonapeptides, requiring the formation of two new peptide bonds. Thus, host defense cells possess mechanisms for synthesis and granular packaging of macrocyclic antibiotic peptides that are components of the phagocyte antimicrobial armamentarium.

Original languageEnglish (US)
Pages (from-to)498-502
Number of pages5
JournalScience
Volume286
Issue number5439
DOIs
StatePublished - Oct 15 1999

ASJC Scopus subject areas

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    Tang, Y. Q., Yuan, J., Ösapay, G., Ösapay, K., Tran, D., Miller, C. J., Ouellette, A. J., & Selsted, M. E. (1999). A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science, 286(5439), 498-502. https://doi.org/10.1126/science.286.5439.498